Drug–Protein Interaction: Spectroscopic and Theoretical Analysis on the Association between HSA and 1,4-Naphthoquinone Derivatives

Resumo

interaction between human serum albumin (HSA) and two biologically active 1,4-naphthoquinone derivatives (FNP and FNP4Br) was studied by circular dichroism, steady-state and time-resolved fluorescence under biological conditions at 305 K, 310 K and 315 K. In order to offer a molecular level explanation, molecular docking calculations were carried out. A ground state association between albumin and the samples was observed by spectroscopic studies. The binding is spontaneous, moderate, can perturb the secondary structure of the albumin and increase the hydrophobicity around the Trp-214 residue, probably due the hydrophobic effect. Thermodynamic parameters and molecular docking results suggest hydrogen bonding and hydrophobic interactions as the main binding forces for the association HSA:FNP and HSA:FNP4Br.